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Protein

Molybdopterin synthase catalytic subunit

Gene

moaE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Converts molybdopterin precursor Z to molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD.

Catalytic activityi

Cyclic pyranopterin phosphate + 2 [molybdopterin-synthase sulfur-carrier protein]-Gly-NH-CH(2)-C(O)SH + H2O = molybdopterin + 2 [molybdopterin-synthase sulfur-carrier protein].1 Publication

Pathwayi: molybdopterin biosynthesis

This protein is involved in the pathway molybdopterin biosynthesis, which is part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the pathway molybdopterin biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei119 – 1191SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Molybdenum cofactor biosynthesis

Enzyme and pathway databases

BioCyciEcoCyc:EG11598-MONOMER.
ECOL316407:JW0768-MONOMER.
MetaCyc:EG11598-MONOMER.
BRENDAi2.8.1.12. 2026.
UniPathwayiUPA00344.

Names & Taxonomyi

Protein namesi
Recommended name:
Molybdopterin synthase catalytic subunit (EC:2.8.1.12)
Alternative name(s):
MPT synthase subunit 2
Molybdenum cofactor biosynthesis protein E
Molybdopterin-converting factor large subunit
Molybdopterin-converting factor subunit 2
Gene namesi
Name:moaE
Synonyms:chlA5
Ordered Locus Names:b0785, JW0768
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11598. moaE.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi34 – 341F → A: 4-fold lower activity than wild-type. 1 Publication
Mutagenesisi39 – 391R → A: 24-fold lower activity than wild-type. 1 Publication
Mutagenesisi115 – 1151M → A: 4-fold lower activity than wild-type. 1 Publication
Mutagenesisi119 – 1191K → A: No activity. 1 Publication
Mutagenesisi126 – 1261K → A: 58-fold lower activity than wild-type. Accumulates large quantities of reaction intermediate. 1 Publication
Mutagenesisi128 – 1281E → K: 17-fold lower activity than wild-type. 1 Publication
Mutagenesisi140 – 1401R → A: 2-fold lower activity than wild-type. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 150149Molybdopterin synthase catalytic subunitPRO_0000163082Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki119 – 119Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in MoaD)

Keywords - PTMi

Isopeptide bond

Proteomic databases

EPDiP30749.
PaxDbiP30749.
PRIDEiP30749.

Expressioni

Inductioni

By anaerobiosis, repressed by the molybdenum cofactor.

Interactioni

Subunit structurei

Heterotetramer of 2 MoaD subunits and 2 MoaE subunits. Also stable as homodimer. The enzyme changes between these two forms during catalysis.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
moaDP307487EBI-554376,EBI-554366

Protein-protein interaction databases

BioGridi4262180. 10 interactions.
DIPiDIP-10232N.
IntActiP30749. 21 interactions.
MINTiMINT-155543.
STRINGi511145.b0785.

Structurei

Secondary structure

1
150
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 118Combined sources
Helixi15 – 228Combined sources
Beta strandi30 – 378Combined sources
Beta strandi50 – 545Combined sources
Helixi56 – 7318Combined sources
Beta strandi76 – 849Combined sources
Beta strandi86 – 883Combined sources
Beta strandi93 – 10311Combined sources
Helixi104 – 12118Combined sources
Beta strandi124 – 1307Combined sources
Beta strandi133 – 1364Combined sources
Helixi141 – 1488Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FM0X-ray1.45E1-150[»]
1FMAX-ray1.58E1-150[»]
1NVIX-ray1.90E1-150[»]
1NVJX-ray2.15A/B/C/D/E/F1-140[»]
3BIIX-ray2.50E2-150[»]
ProteinModelPortaliP30749.
SMRiP30749. Positions 2-127.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30749.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni37 – 393Substrate bindingBy similarity
Regioni103 – 1042Substrate bindingBy similarity
Regioni126 – 1283Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the MoaE family.Curated

Phylogenomic databases

eggNOGiENOG4108ZAF. Bacteria.
COG0314. LUCA.
HOGENOMiHOG000280876.
InParanoidiP30749.
KOiK03635.
OMAiRERWPLN.
OrthoDBiEOG6KMBD9.
PhylomeDBiP30749.

Family and domain databases

Gene3Di3.90.1170.40. 1 hit.
InterProiIPR003448. Mopterin_biosynth_MoaE.
[Graphical view]
PANTHERiPTHR23404:SF2. PTHR23404:SF2. 1 hit.
PfamiPF02391. MoaE. 1 hit.
[Graphical view]
SUPFAMiSSF54690. SSF54690. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P30749-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAETKIVVGP QPFSVGEEYP WLAERDEDGA VVTFTGKVRN HNLGDSVNAL
60 70 80 90 100
TLEHYPGMTE KALAEIVDEA RNRWPLGRVT VIHRIGELWP GDEIVFVGVT
110 120 130 140 150
SAHRSSAFEA GQFIMDYLKT RAPFWKREAT PEGDRWVEAR ESDQQAAKRW
Length:150
Mass (Da):16,981
Last modified:January 23, 2007 - v3
Checksum:i6E40776E5A6E85BB
GO

Mass spectrometryi

Molecular mass is 16849.7±0.7 Da from positions 2 - 150. Determined by ESI. 1 Publication
Molecular mass is 16851 Da from positions 2 - 150. Determined by API. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70420 Genomic DNA. Translation: CAA49865.1.
U00096 Genomic DNA. Translation: AAC73872.1.
AP009048 Genomic DNA. Translation: BAA35443.1.
PIRiS35002. S31883.
RefSeqiNP_415306.1. NC_000913.3.
WP_000852296.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73872; AAC73872; b0785.
BAA35443; BAA35443; BAA35443.
GeneIDi945399.
KEGGiecj:JW0768.
eco:b0785.
PATRICi32116771. VBIEscCol129921_0811.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70420 Genomic DNA. Translation: CAA49865.1.
U00096 Genomic DNA. Translation: AAC73872.1.
AP009048 Genomic DNA. Translation: BAA35443.1.
PIRiS35002. S31883.
RefSeqiNP_415306.1. NC_000913.3.
WP_000852296.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FM0X-ray1.45E1-150[»]
1FMAX-ray1.58E1-150[»]
1NVIX-ray1.90E1-150[»]
1NVJX-ray2.15A/B/C/D/E/F1-140[»]
3BIIX-ray2.50E2-150[»]
ProteinModelPortaliP30749.
SMRiP30749. Positions 2-127.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262180. 10 interactions.
DIPiDIP-10232N.
IntActiP30749. 21 interactions.
MINTiMINT-155543.
STRINGi511145.b0785.

Proteomic databases

EPDiP30749.
PaxDbiP30749.
PRIDEiP30749.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73872; AAC73872; b0785.
BAA35443; BAA35443; BAA35443.
GeneIDi945399.
KEGGiecj:JW0768.
eco:b0785.
PATRICi32116771. VBIEscCol129921_0811.

Organism-specific databases

EchoBASEiEB1555.
EcoGeneiEG11598. moaE.

Phylogenomic databases

eggNOGiENOG4108ZAF. Bacteria.
COG0314. LUCA.
HOGENOMiHOG000280876.
InParanoidiP30749.
KOiK03635.
OMAiRERWPLN.
OrthoDBiEOG6KMBD9.
PhylomeDBiP30749.

Enzyme and pathway databases

UniPathwayiUPA00344.
BioCyciEcoCyc:EG11598-MONOMER.
ECOL316407:JW0768-MONOMER.
MetaCyc:EG11598-MONOMER.
BRENDAi2.8.1.12. 2026.

Miscellaneous databases

EvolutionaryTraceiP30749.
PROiP30749.

Family and domain databases

Gene3Di3.90.1170.40. 1 hit.
InterProiIPR003448. Mopterin_biosynth_MoaE.
[Graphical view]
PANTHERiPTHR23404:SF2. PTHR23404:SF2. 1 hit.
PfamiPF02391. MoaE. 1 hit.
[Graphical view]
SUPFAMiSSF54690. SSF54690. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular genetic analysis of the moa operon of Escherichia coli K-12 required for molybdenum cofactor biosynthesis."
    Rivers S.L., McNairn E., Blasco F., Giordano G., Boxer D.H.
    Mol. Microbiol. 8:1071-1081(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "The biosynthesis of molybdopterin in Escherichia coli. Purification and characterization of the converting factor."
    Pitterle D.M., Rajagopalan K.V.
    J. Biol. Chem. 268:13499-13505(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-16, CHARACTERIZATION, MASS SPECTROMETRY.
  6. "Mechanistic and mutational studies of Escherichia coli molybdopterin synthase clarify the final step of molybdopterin biosynthesis."
    Wuebbens M.M., Rajagopalan K.V.
    J. Biol. Chem. 278:14523-14532(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, KINETIC ANALYSIS, DISCOVERY OF REACTION INTERMEDIATE, MUTAGENESIS OF PHE-34; ARG-39; MET-115; LYS-119; LYS-126; GLU-128 AND ARG-140.
  7. "Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation."
    Rudolph M.J., Wuebbens M.M., Rajagopalan K.V., Schindelin H.
    Nat. Struct. Biol. 8:42-46(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEXES WITH MOAD, CROSS-LINKING TO MOAD, MASS SPECTROMETRY, SUBUNIT.
  8. "Structural studies of molybdopterin synthase provide insights into its catalytic mechanism."
    Rudolph M.J., Wuebbens M.M., Turque O., Rajagopalan K.V., Schindelin H.
    J. Biol. Chem. 278:14514-14522(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH MOAD-THIOCARBOXYLATE, REACTION MECHANISM.

Entry informationi

Entry nameiMOAE_ECOLI
AccessioniPrimary (citable) accession number: P30749
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 143 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The cross-link is not seen in all structures of the MoaE-MoaD complex.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.